Properties of 5-Hydroxyvalerate CoA-Transferase fromClostridium aminovalericum
- 1 January 1990
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 371 (2) , 1077-1082
- https://doi.org/10.1515/bchm3.1990.371.2.1077
Abstract
5-Hydroxyvalerate CoA-transferase from Clostridium aminovalericum, strain T2-7, was purified approximately 100-fold to homogeneity. The molecular mass of the native enzyme was determined by three different methods to be 178 .+-. 11 kDa; that of the subunit was 47 kDa, indicating a homotetrameric structure. The following CoA esters acted as substrates (decreasing specificity, V/Km): 5-hydroxyvaleryl-CoA > propionyl-CoA > acetyl-CoA > (Z)-5-hydroxy-2-pentenoyl-CoA > butyryl-CoA > valeryl-CoA. 4-Pentenoate and 3-pentenoate were also activated by acetyl-CoA to the corresponding CoA esters, whereas crotonate, (E)-5-hydroxy-2-penteonate, (E)-2-pentenoate and 2,4-pentadienoate were not attacked. 5-Hydroxyvalerate CoA-transferase showed ping-pong kinetics and was inactivated by sodium boranate only in the presence of a CoA substrate. This indicated the formation of a thiolester between a specific carboxyl group of of the enzyme and CoASH during the course of the reaction. The CoA-transferase was inhibited by ATP and CTP, slightly by ADP, GTP and UTP, but not by AMP. The inhibition by ATP was competitive towards CoA esters and non-competitive towards acetate.This publication has 6 references indexed in Scilit:
- Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenesJournal of Bacteriology, 1990
- Enzymatic reactions in the degradation of 5-aminovalerate by Clostridium aminovalericum.Journal of Biological Chemistry, 1987
- Glutaconate CoA‐Transferase from Acidaminococcus fermentansEuropean Journal of Biochemistry, 1981
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Acetic Anhydride: an Intermediate. Analogue in the Acyl‐Exchange Reaction of Citramalate LyaseEuropean Journal of Biochemistry, 1976
- Purification and properties of Escherichia coli coenzyme A-transferaseArchives of Biochemistry and Biophysics, 1975